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Title: Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice

Abstract

Self-assembling proteins offer a potential means of creating nanostructures with complex structure and function. However, using self-assembly to create nanostructures with long-range order whose size is tunable is challenging, because the kinetics and thermodynamics of protein interactions depend sensitively on solution conditions. Here we systematically investigate the impact of varying solution conditions on the self-assembly of SbpA, a surface-layer protein from Lysinibacillus sphaericus that forms two-dimensional nanosheets. Using high-throughput light scattering measurements, we mapped out diagrams that reveal the relative yield of self-assembly of nanosheets over a wide range of concentrations of SbpA and Ca 2+. These diagrams revealed a localized region of optimum yield of nanosheets at intermediate Ca 2+ concentration. Replacement of Mg 2+ or Ba 2+ for Ca 2+ indicates that Ca 2+ acts both as a specific ion that is required to induce self-assembly and as a general divalent cation. In addition, we use competitive titration experiments to find that 5 Ca 2+ bind to SbpA with an affinity of 67.1 ± 0.3 μM. Finally, we show via modeling that nanosheet assembly occurs by growth from a negligibly small critical nucleus. We also chart the dynamics of nanosheet size over a variety of conditions. In conclusion,more » our results demonstrate control of the dynamics and size of the self-assembly of a nanostructured lattice, the constituents of which are one of a class of building blocks able to form novel hybrid nanomaterials.« less

Authors:
; ;  [1];  [2]; ;
  1. Department of Chemical and Biomolecular Engineering, UC Berkeley, Berkeley, California 94720-1462, United States
  2. Department of Chemistry, UC Berkeley, Berkeley, California 94720-1460, United States
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1168700
Alternate Identifier(s):
OSTI ID: 1257359
Grant/Contract Number:  
AC02-05CH11231; R01GM105404
Resource Type:
Published Article
Journal Name:
ACS Nano
Additional Journal Information:
Journal Name: ACS Nano Journal Volume: 9 Journal Issue: 1; Journal ID: ISSN 1936-0851
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English
Subject:
77 NANOSCIENCE AND NANOTECHNOLOGY; protein interactions; biomaterials; nanostructures; self-assembly dynamics; Ca2+ binding

Citation Formats

Rad, Behzad, Haxton, Thomas K., Shon, Albert, Shin, Seong-Ho, Whitelam, Stephen, and Ajo-Franklin, Caroline M. Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice. United States: N. p., 2014. Web. doi:10.1021/nn502992x.
Rad, Behzad, Haxton, Thomas K., Shon, Albert, Shin, Seong-Ho, Whitelam, Stephen, & Ajo-Franklin, Caroline M. Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice. United States. doi:10.1021/nn502992x.
Rad, Behzad, Haxton, Thomas K., Shon, Albert, Shin, Seong-Ho, Whitelam, Stephen, and Ajo-Franklin, Caroline M. Wed . "Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice". United States. doi:10.1021/nn502992x.
@article{osti_1168700,
title = {Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice},
author = {Rad, Behzad and Haxton, Thomas K. and Shon, Albert and Shin, Seong-Ho and Whitelam, Stephen and Ajo-Franklin, Caroline M.},
abstractNote = {Self-assembling proteins offer a potential means of creating nanostructures with complex structure and function. However, using self-assembly to create nanostructures with long-range order whose size is tunable is challenging, because the kinetics and thermodynamics of protein interactions depend sensitively on solution conditions. Here we systematically investigate the impact of varying solution conditions on the self-assembly of SbpA, a surface-layer protein from Lysinibacillus sphaericus that forms two-dimensional nanosheets. Using high-throughput light scattering measurements, we mapped out diagrams that reveal the relative yield of self-assembly of nanosheets over a wide range of concentrations of SbpA and Ca2+. These diagrams revealed a localized region of optimum yield of nanosheets at intermediate Ca2+ concentration. Replacement of Mg2+ or Ba2+ for Ca2+ indicates that Ca2+ acts both as a specific ion that is required to induce self-assembly and as a general divalent cation. In addition, we use competitive titration experiments to find that 5 Ca2+ bind to SbpA with an affinity of 67.1 ± 0.3 μM. Finally, we show via modeling that nanosheet assembly occurs by growth from a negligibly small critical nucleus. We also chart the dynamics of nanosheet size over a variety of conditions. In conclusion, our results demonstrate control of the dynamics and size of the self-assembly of a nanostructured lattice, the constituents of which are one of a class of building blocks able to form novel hybrid nanomaterials.},
doi = {10.1021/nn502992x},
journal = {ACS Nano},
number = 1,
volume = 9,
place = {United States},
year = {2014},
month = {12}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: 10.1021/nn502992x

Citation Metrics:
Cited by: 11 works
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Works referencing / citing this record:

Structure of S-layer protein Sap reveals a mechanism for therapeutic intervention in anthrax
journal, July 2019

  • Fioravanti, Antonella; Van Hauwermeiren, Filip; Van der Verren, Sander E.
  • Nature Microbiology, Vol. 4, Issue 11
  • DOI: 10.1038/s41564-019-0499-1

Structure of S-layer protein Sap reveals a mechanism for therapeutic intervention in anthrax
journal, July 2019

  • Fioravanti, Antonella; Van Hauwermeiren, Filip; Van der Verren, Sander E.
  • Nature Microbiology, Vol. 4, Issue 11
  • DOI: 10.1038/s41564-019-0499-1